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Protein

Bifunctional beta-D-glucosidase/beta-D-fucosidase

Gene
N/A
Organism
Bifidobacterium breve
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional beta-D-glucosidase/beta-D-fucosidase. Activity towards pNP-beta-D-fucoside is about 80-85% of the activity towards pNP-beta-D-glucoside. Also has slight activity (less than 10%) towards pNP-beta-D-galactoside, and very low activity (less than 1%) towards pNP-beta-D-xyloside. Hydrolyzes laminaribiose, sophorose, cellobiose and gentobiose. Not active against maltose, pNP-alpha-D-glucoside or pNP-beta-L-fucoside.2 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.2 Publications
Hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides.2 Publications

Enzyme regulationi

Inhibited by Cu2+, Ag+ and Hg+, but not by other cations such as Mg2+, Ca2+, Mn2+ and Co2+. Inhibited by 1-amino-1-deoxy-D-glucose and p-chloromercuribenzoic acid, but not by EDTA or dithiothreitol. Inhibited by the disaccharides sucrose, lactose and cellobiose. The monosaccharides D-fructose, D-mannose, D-xylose and D-glucose increase the beta-D-fucosidase activity, but not the beta-D-glucosidase activity. D-glucose inhibits the beta-D-glucosidase activity, but promotes the beta-D-fucosidase activity. D-fucose inhibits the beta-D-glucosidase activity and does not significantly affect the beta-D-fucosidase activity.1 Publication

Kineticsi

  1. KM=1.3 mM for pNP-beta-D-glucoside2 Publications
  2. KM=0.7 mM for pNP-beta-D-fucoside2 Publications

    pH dependencei

    Optimum pH is 5.5 with pNP-beta-D-glucoside as a substrate. Retains more than 90% of its activity between pH 5.0 and 7.0. Retains 70% of its activity at pH 4.5 and 8.5.2 Publications

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius with pNP-beta-D-glucoside as a substrate. Retains 60% of its activity after 10 minutes incubation at 50 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei168 – 1681Proton donorBy similarity
    Active sitei362 – 3621NucleophilePROSITE-ProRule annotationBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional beta-D-glucosidase/beta-D-fucosidase (EC:3.2.1.21, EC:3.2.1.38)
    OrganismiBifidobacterium breve
    Taxonomic identifieri1685 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaBifidobacterialesBifidobacteriaceaeBifidobacterium

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 460459Bifunctional beta-D-glucosidase/beta-D-fucosidase1 PublicationPRO_0000395428Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP94248.
    SMRiP94248. Positions 2-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Sequence Analysis

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR017736. Glyco_hydro_1_beta-glucosidase.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    TIGRFAMsiTIGR03356. BGL. 1 hit.
    PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P94248-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTMIFPKGFM FGTATAAYQI EGAVAEGGRT PSIWDTFSHT GHTLNGDTGD
    60 70 80 90 100
    VADDFYHRWE DDLKLLRDLG VNAYRFSIGI PRVIPTPDGK PNQEGLDFYS
    110 120 130 140 150
    RIVDRLLEYG IAPIVTLYHW DLPQYMASGD GREGGWLERE TAYRIADYAG
    160 170 180 190 200
    IVAKCLGDRV HTYTTLNEPW CSAHLSYGGT EHAPGLGAGP LAFRAAHHLN
    210 220 230 240 250
    LAHGLMCEAV RAEAGAKPGL SVTLNLQICR GDADAVHRVD LIGNRVFLDP
    260 270 280 290 300
    MLRGRYPDEL FSITKGICDW GFVCDGDLDL IHQPIDVLGL NYYSTNLVKM
    310 320 330 340 350
    SDRPQFPQST EASTAPGASD VDWLPTAGPH TEMGWNIDPD ALYETLVRLN
    360 370 380 390 400
    DNYPGMPLVV TENGMACPDK VEVGTDGVKM VHDNDRIDYL RRHLEAVYRA
    410 420 430 440 450
    IEEGTDVRGY FAWSLMDNFE WAFGYSKRFG LTYVDYESQE RVKKDSFDWY
    460
    RRFIADHSAR
    Length:460
    Mass (Da):51,514
    Last modified:May 1, 1997 - v1
    Checksum:i5FD80CB8AB6888A9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D88311 Genomic DNA. Translation: BAA19881.1.
    PIRiJC5137.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D88311 Genomic DNA. Translation: BAA19881.1.
    PIRiJC5137.

    3D structure databases

    ProteinModelPortaliP94248.
    SMRiP94248. Positions 2-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR017736. Glyco_hydro_1_beta-glucosidase.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    TIGRFAMsiTIGR03356. BGL. 1 hit.
    PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Cloning and nucleotide sequence of the beta-D-glucosidase gene from Bifidobacterium breve clb, and expression of beta-D-glucosidase activity in Escherichia coli."
      Nunoura N., Ohdan K., Tanaka K., Tamaki H., Yano T., Inui M., Yukawa H., Yamamoto K., Kumagai H.
      Biosci. Biotechnol. Biochem. 60:2011-2018(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    2. "Purification and characterization of beta-D-glucosidase (beta-D-fucosidase) from Bifidobacterium breve clb acclimated to cellobiose."
      Nunoura N., Ohdan K., Yano T., Yamamoto K., Kumagai H.
      Biosci. Biotechnol. Biochem. 60:188-193(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-30, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiBGLFU_BIFBR
    AccessioniPrimary (citable) accession number: P94248
    Secondary accession number(s): O08487
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: May 1, 1997
    Last modified: June 24, 2015
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.